Glycine-rich loop of mitochondrial processing peptidase α-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20

0340832 - MBÚ 2011 RIV GB eng J - Journal Article
Dvořáková-Holá, Klára - Matušková, Anna - Kubala, M. - Otyepka, M. - Kučera, Tomáš - Večeř, J. - Heřman, P. - Parkhomenko, Natalia - Kutejová, E. - Janata, Jiří
Glycine-rich loop of mitochondrial processing peptidase α-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20.
Journal of Molecular Biology. Roč. 396, č. 5 (2010), s. 1197-1210. ISSN 0022-2836. E-ISSN 1089-8638
R&D Projects: GA AV ČR IAA501110631
Institutional research plan: CEZ:AV0Z50200510
Keywords : mitochondrial processing peptidase * presequence * substrate recognition
Subject RIV: EE - Microbiology, Virology
Impact factor: 4.008, year: 2010

Tryptophan fluorescence measurements were used to characterize the local dynamics of the highly conserved glycine-rich loop (GRL) of the mitochondrial processing peptidase (MPP) subunit in the presence of the substrate precursor. Reporter tryptophan residue was introduced into the GRL of the yeast MPP (Y299W) or at a proximal site (Y303W). Timeresolved and steady-state fluorescence spectroscopy demonstrated that for Trp299, the primary contact with the yeast malate dehydrogenase precursor evokes a change of the local GRL mobility. Moreover, time-resolved measurements showed that a functionless MPP with a single-residue deletion in the loop (Y303W/G292) is defective particularly in the primary contact with substrate
Permanent Link: http://hdl.handle.net/11104/0183995